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本文引用的文献

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Membrane-protein interactions in cell signaling and membrane trafficking.细胞信号传导与膜运输中的膜蛋白相互作用。
Annu Rev Biophys Biomol Struct. 2005;34:119-51. doi: 10.1146/annurev.biophys.33.110502.133337.
2
Membrane binding assays for peripheral proteins.外周蛋白的膜结合测定
Anal Biochem. 2001 Sep 15;296(2):153-61. doi: 10.1006/abio.2001.5225.
3
Effects of excluded surface area and adsorbate clustering on surface adsorption of proteins I. Equilibrium models.排除表面积和吸附质聚集对蛋白质表面吸附的影响I. 平衡模型
Biophys Chem. 2000 Aug 30;86(2-3):239-47. doi: 10.1016/s0301-4622(00)00151-4.
4
A phospholipase A2 kinetic and binding assay using phospholipid-coated hydrophobic beads.一种使用磷脂包被的疏水微珠的磷脂酶A2动力学和结合测定法。
Anal Biochem. 1997 Jul 15;250(1):109-16. doi: 10.1006/abio.1997.2200.
5
Adsorption of globular proteins on locally planar surfaces: models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria.球状蛋白质在局部平面表面上的吸附:关于排除表面积和吸附蛋白质聚集对吸附平衡影响的模型
Biophys J. 1996 Nov;71(5):2367-74. doi: 10.1016/S0006-3495(96)79430-4.
6
Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles.磷酸化、高离子强度和钙调蛋白可逆转MARCKS与磷脂囊泡的结合。
J Biol Chem. 1994 Nov 11;269(45):28214-9.
7
A method for probing the affinity of peptides for amphiphilic surfaces.一种探测肽与两亲性表面亲和力的方法。
Anal Biochem. 1985 Oct;150(1):131-40. doi: 10.1016/0003-2697(85)90451-8.

外周蛋白膜结合平衡分析:结合蛋白排除面积的考虑。

Analysis of membrane binding equilibria of peripheral proteins: allowance for excluded area of bound protein.

机构信息

Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, MD 20892, USA.

出版信息

Anal Biochem. 2010 Feb 15;397(2):247-9. doi: 10.1016/j.ab.2009.10.023. Epub 2009 Nov 1.

DOI:10.1016/j.ab.2009.10.023
PMID:19837044
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2812583/
Abstract

When peripheral proteins bind to phospholipid membranes lacking discrete binding sites, steric repulsion between bound protein molecules may result in a reduction of the surface area available to additional bound protein by an amount significantly greater than the actual area occupied by bound protein. An approximate treatment of this effect demonstrates that neglect of area exclusion by bound protein may lead to significant errors in the evaluation of equilibrium association constants and the fractional coverage of membrane surface area.

摘要

当外周蛋白与缺乏离散结合位点的磷脂膜结合时,结合蛋白分子之间的空间排斥可能导致可用于额外结合蛋白的表面积减少,其减少量明显大于结合蛋白实际占据的面积。对这种效应的近似处理表明,忽略结合蛋白的面积排除可能导致在评估平衡缔合常数和膜表面积的分数覆盖时产生显著误差。